ID   ARSC2_STAHJ             Reviewed;         131 AA.
AC   Q4LAA8;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   16-JUN-2009, entry version 30.
DE   RecName: Full=Protein arsC 2;
DE   AltName: Full=Arsenate reductase 2;
DE            EC=1.20.4.-;
DE   AltName: Full=Arsenical pump modifier 2;
DE   AltName: Full=Low molecular weight protein-tyrosine-phosphatase 2;
DE            EC=3.1.3.48;
GN   Name=arsC2; OrderedLocusNames=SH0108;
OS   Staphylococcus haemolyticus (strain JCSC1435).
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=279808;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16237012; DOI=10.1128/JB.187.21.7292-7308.2005;
RA   Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA   Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S.,
RA   Lee J.C., Hiramatsu K.;
RT   "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT   extreme plasticity of its genome and the evolution of human-colonizing
RT   staphylococcal species.";
RL   J. Bacteriol. 187:7292-7308(2005).
CC   -!- FUNCTION: Reduces arsenate [As(V)] to arsenite [As(III)] and
CC       dephosphorylates tyrosine phosphorylated proteins, low-MW aryl
CC       phosphates and natural and synthetic acyl phosphates. Could switch
CC       between different functions in different circumstances (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
CC       tyrosine + phosphate.
CC   -!- CATALYTIC ACTIVITY: Arsenate + thioredoxin = arsenite +
CC       thioredoxin disulfide + H(2)O.
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SIMILARITY: Belongs to the low molecular weight phosphotyrosine
CC       protein phosphatase superfamily. ArsC family.
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DR   EMBL; AP006716; BAE03417.1; -; Genomic_DNA.
DR   RefSeq; YP_252023.1; -.
DR   SMR; Q4LAA8; 1-131.
DR   GeneID; 3482396; -.
DR   GenomeReviews; AP006716_GR; SH0108.
DR   KEGG; sha:SH0108; -.
DR   NMPDR; fig|279808.3.peg.120; -.
DR   HOGENOM; Q4LAA8; -.
DR   OMA; Q4LAA8; EMRIVIT.
DR   BioCyc; SHAE279808:SH0108-MON; -.
DR   GO; GO:0030612; F:arsenate reductase (thioredoxin) activity; IEA:HAMAP.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:HAMAP.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0006470; P:protein amino acid dephosphorylation; IEA:InterPro.
DR   GO; GO:0046685; P:response to arsenic; IEA:UniProtKB-KW.
DR   HAMAP; MF_01624; -; 1.
DR   InterPro; IPR014064; Arsenate_reductase_StaphA.
DR   InterPro; IPR017867; Tyr_phospatase_low_mol_wt.
DR   PANTHER; PTHR11717; Low_mwt_PTPase; 1.
DR   Pfam; PF01451; LMWPc; 1.
DR   SMART; SM00226; LMWPc; 1.
DR   TIGRFAMs; TIGR02691; arsC_pI258_fam; 1.
PE   3: Inferred from homology;
KW   Arsenical resistance; Complete proteome; Disulfide bond; Hydrolase;
KW   Oxidoreductase; Redox-active center.
FT   CHAIN         1    131       Protein arsC 2.
FT                                /FTId=PRO_0000162531.
FT   ACT_SITE     10     10       Nucleophile; for reductase activity and
FT                                phosphatase activity (By similarity).
FT   ACT_SITE     82     82       Nucleophile; for reductase activity (By
FT                                similarity).
FT   ACT_SITE     89     89       Nucleophile; for reductase activity (By
FT                                similarity).
FT   DISULFID     10     82       Redox-active; alternate (By similarity).
FT   DISULFID     82     89       Redox-active; alternate (By similarity).
SQ   SEQUENCE   131 AA;  14683 MW;  4049813AF5BDB6F7 CRC64;
     MDKKTIYFIC TGNSCRSQMA EGWGKKILGD EWQVYSGGIE AHGVNPKAIE AMKEVGIDIS
     NHTSNLIDKN ILNQSDLVVT LCSDADNNCP ILPPNVKKEH WGFDDPAGKP WSEFQRVRDE
     IKTAIESFKT R
//